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The tubulin code: Molecular components, readout mechanisms, and functions
Microtubules are cytoskeletal filaments that are dynamically assembled from α/β-tubulin heterodimers. The primary sequence and structure of the tubulin proteins and, consequently, the properties and architecture of microtubules are highly conserved in eukaryotes. Despite this conservation, tubulin i...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Rockefeller University Press
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4137062/ https://www.ncbi.nlm.nih.gov/pubmed/25135932 http://dx.doi.org/10.1083/jcb.201406055 |
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author | Janke, Carsten |
author_facet | Janke, Carsten |
author_sort | Janke, Carsten |
collection | PubMed |
description | Microtubules are cytoskeletal filaments that are dynamically assembled from α/β-tubulin heterodimers. The primary sequence and structure of the tubulin proteins and, consequently, the properties and architecture of microtubules are highly conserved in eukaryotes. Despite this conservation, tubulin is subject to heterogeneity that is generated in two ways: by the expression of different tubulin isotypes and by posttranslational modifications (PTMs). Identifying the mechanisms that generate and control tubulin heterogeneity and how this heterogeneity affects microtubule function are long-standing goals in the field. Recent work on tubulin PTMs has shed light on how these modifications could contribute to a “tubulin code” that coordinates the complex functions of microtubules in cells. |
format | Online Article Text |
id | pubmed-4137062 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-41370622015-02-18 The tubulin code: Molecular components, readout mechanisms, and functions Janke, Carsten J Cell Biol Reviews Microtubules are cytoskeletal filaments that are dynamically assembled from α/β-tubulin heterodimers. The primary sequence and structure of the tubulin proteins and, consequently, the properties and architecture of microtubules are highly conserved in eukaryotes. Despite this conservation, tubulin is subject to heterogeneity that is generated in two ways: by the expression of different tubulin isotypes and by posttranslational modifications (PTMs). Identifying the mechanisms that generate and control tubulin heterogeneity and how this heterogeneity affects microtubule function are long-standing goals in the field. Recent work on tubulin PTMs has shed light on how these modifications could contribute to a “tubulin code” that coordinates the complex functions of microtubules in cells. The Rockefeller University Press 2014-08-18 /pmc/articles/PMC4137062/ /pubmed/25135932 http://dx.doi.org/10.1083/jcb.201406055 Text en © 2014 Janke This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Reviews Janke, Carsten The tubulin code: Molecular components, readout mechanisms, and functions |
title | The tubulin code: Molecular components, readout mechanisms, and functions |
title_full | The tubulin code: Molecular components, readout mechanisms, and functions |
title_fullStr | The tubulin code: Molecular components, readout mechanisms, and functions |
title_full_unstemmed | The tubulin code: Molecular components, readout mechanisms, and functions |
title_short | The tubulin code: Molecular components, readout mechanisms, and functions |
title_sort | tubulin code: molecular components, readout mechanisms, and functions |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4137062/ https://www.ncbi.nlm.nih.gov/pubmed/25135932 http://dx.doi.org/10.1083/jcb.201406055 |
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